Phosphorylation of SHP-2 regulates interactions between the endoplasmic reticulum and focal adhesions to restrict interleukin-1-induced Ca2+ signaling.

Wang, Qin; Herrera Abreu, Maria Teresa; Siminovitch, Katherine; Downey, Gregory P; McCulloch, Christopher A

Wang, Qin; Herrera Abreu, Maria Teresa; Siminovitch, Katherine; Downey, Gregory P; McCulloch, Christopher A.

Affiliation

Wang Q; Canadian Institutes of Health Research Group in Matrix Dynamics, University of Toronto, Toronto, Ontario M5S 3E2, Canada.

J Biol Chem ; 281(41): 31093-105, 2006 Oct 13.

Article in En | MEDLINE | ID: mdl-16905534

Subject(s)

Calcium/metabolism; Endoplasmic Reticulum/metabolism; Interleukin-1/metabolism; Intracellular Signaling Peptides and Proteins/chemistry; Protein Tyrosine Phosphatases/chemistry; Animals; Cell Membrane/metabolism; Fibroblasts/metabolism; Focal Adhesions/chemistry; Humans; Intracellular Signaling Peptides and Proteins/metabolism; Phosphorylation; Protein Binding; Protein Tyrosine Phosphatase, Non-Receptor Type 1; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Protein Tyrosine Phosphatases/metabolism; Rats; Signal Transduction; Subcellular Fractions/metabolism

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Collection: 01-internacional Database: MEDLINE Main subject: Calcium / Interleukin-1 / Protein Tyrosine Phosphatases / Intracellular Signaling Peptides and Proteins / Endoplasmic Reticulum Limits: Animals / Humans Language: En Journal: J Biol Chem Year: 2006 Document type: Article Affiliation country: Canada Country of publication: United States

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